Structural elements of primary CCR5-using HIV-1 gp120 proteins influencing sensitivity and resistance to the broadly neutralizing monoclonal antibody b12 (Q62572413)

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English	Structural elements of primary CCR5-using HIV-1 gp120 proteins influencing sensitivity and resistance to the broadly neutralizing monoclonal antibody b12	article

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8 February 2020

Structural elements of primary CCR5-using HIV-1 gp120 proteins influencing sensitivity and resistance to the broadly neutralizing monoclonal antibody b12 (English)

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8 February 2020

Jasminka Sterjovski

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8 February 2020

Paul A. Ramsland

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8 February 2020

Steven L Wesselingh

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Steve L Wesselingh

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8 February 2020

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Anne Ellett

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8 February 2020

Melissa J Churchill

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8 February 2020

Paul R Gorry

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8 February 2020

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19 July 2012

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8 February 2020

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8 February 2020

432

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8 February 2020

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8 February 2020

394-404

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8 February 2020

Computational prediction of the cross-reactive neutralizing epitope corresponding to the [corrected] monclonal [corrected] antibody b12 specific for HIV-1 gp120.

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The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus

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Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: antigenicity, biophysics, and immunogenicity

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HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5

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Natural resistance of human immunodeficiency virus type 1 to the CD4bs antibody b12 conferred by a glycan and an arginine residue close to the CD4 binding loop

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Loss of the N-linked glycosylation site at position 386 in the HIV envelope V4 region enhances macrophage tropism and is associated with dementia.

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Changes in the V3 region of gp120 contribute to unusually broad coreceptor usage of an HIV-1 isolate from a CCR5 Delta32 heterozygote.

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Increased CCR5 affinity and reduced CCR5/CD4 dependence of a neurovirulent primary human immunodeficiency virus type 1 isolate.

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Genetic and functional analysis of R5X4 human immunodeficiency virus type 1 envelope glycoproteins derived from two individuals homozygous for the CCR5delta32 allele

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7 January 2021

Tissue-specific sequence alterations in the human immunodeficiency virus type 1 envelope favoring CCR5 usage contribute to persistence of dual-tropic virus in the brain

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7 January 2021

Uncoupling coreceptor usage of human immunodeficiency virus type 1 (HIV-1) from macrophage tropism reveals biological properties of CCR5-restricted HIV-1 isolates from patients with acquired immunodeficiency syndrome

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Inference of macromolecular assemblies from crystalline state

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HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites

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Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates

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7 January 2021

Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

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7 January 2021

Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus

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Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

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Molecular architecture of native HIV-1 gp120 trimers

1 reference

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V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies

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N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies

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A human IgG1 (b12) specific for the CD4 binding site of HIV-1 neutralizes by inhibiting the virus fusion entry process, but b12 Fab neutralizes by inhibiting a postfusion event

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Intrapatient alterations in the human immunodeficiency virus type 1 gp120 V1V2 and V3 regions differentially modulate coreceptor usage, virus inhibition by CC/CXC chemokines, soluble CD4, and the b12 and 2G12 monoclonal antibodies

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Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120.

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Rapid evolution of the neutralizing antibody response to HIV type 1 infection

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A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding

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HIV-1 predisposed to acquiring resistance to maraviroc (MVC) and other CCR5 antagonists in vitro has an inherent, low-level ability to utilize MVC-bound CCR5 for entry

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HIV-1 escape from the CCR5 antagonist maraviroc associated with an altered and less-efficient mechanism of gp120-CCR5 engagement that attenuates macrophage tropism

1 reference

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Comparative protein modelling by satisfaction of spatial restraints

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The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion.

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Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer

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Mobility of the human immunodeficiency virus (HIV) receptor CD4 and coreceptor CCR5 in living cells: implications for HIV fusion and entry events

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1 reference

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CD4-binding site alterations in CCR5-using HIV-1 envelopes influencing gp120-CD4 interactions and fusogenicity

1 reference

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An altered and more efficient mechanism of CCR5 engagement contributes to macrophage tropism of CCR5-using HIV-1 envelopes

1 reference

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CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5.

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CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5.

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Stoichiometry of antibody neutralization of human immunodeficiency virus type 1.

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Characterization of the outer domain of the gp120 glycoprotein from human immunodeficiency virus type 1

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Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers

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Structural definition of a conserved neutralization epitope on HIV-1 gp120

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Molecular features of the broadly neutralizing immunoglobulin G1 b12 required for recognition of human immunodeficiency virus type 1 gp120.

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Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity

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inferred from DOI database lookup

Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS.

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1.

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG.

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2012.06.024

7 January 2021

based on heuristic

inferred from DOI database lookup

Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding

1 reference

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7 January 2021

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inferred from DOI database lookup

Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2012.06.024

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/J.VIROL.2012.06.024

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22818780%20AND%20SRC:MED&resulttype=core&format=json

8 February 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22818780%20AND%20SRC:MED&resulttype=core&format=json

8 February 2020

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